No abstract

Changes of the xanthine and uric acid (UA) levels in rat forebrain following focal cerebral ischemia were studied by reversed-phase HPLC with electrochemical detection. Focal ischemia was induced by occluding the left middle cerebral artery in the rat. The xanthine level in the normal group was 11.50 nmol/g tissue. In the ischemic group, the xanthine concentration in the ischemic hemisphere progressively increased after occlusion and reached a maximum value of 59.42 nmol/g tissue 4 h after operation. The UA level in the normal group was 2.20 nmol/g tissue, whereas in the ischemic group the UA concentration in the ischemic hemisphere gradually increased after occlusion, reaching a value of 38.53 nmol/g tissue 24 h after ischemia. The concentration of UA remained elevated in the ischemic hemisphere until 48 h after occlusion, and reached a maximum value of 38.98 nmol/g tissue. The xanthine and UA levels in the contralateral hemisphere remained unchanged. The xanthine and UA concentrations in the sham-operated group did not show a significant increase after operation. The time course of xanthine and UA levels suggests that in ischemic forebrain UA is formed from xanthine as a product of purine metabolism.

Changes of uric acid level in rat cerebral hemisphere after left middle cerebral artery (MCA) occlusion were studied by reversed-phase HPLC with electrochemical detection. Uric acid level in the normal group was 2.98 nmol/g tissue. Uric acid concentration of the left hemisphere in the left MCA-occluded group progressively increased after occlusion, and reached a maximum value of 67.26 nmol/g tissue 24 h after ischemia. Uric acid levels in the right hemisphere remained unchanged. Uric acid concentration of the left hemisphere in sham-operated group was 9.29 nmol/g tissue 24 h after the operation.

No abstract

No abstract

No abstract

Age-related structural changes in the lens proteins of a normal mouse lens have been monitored in situ by laser Raman spectroscopy. The Raman spectrum of an ICR-strain mouse lens nucleus showed virtually no change in the 550-850- and 900-1800-cm-1 regions as the mouse aged. Lens aging, however, did cause a significant intensity decrease of the Raman band at 880 cm-1 due to tryptophan residues, and the intensity decrease seems to be stepwise. This observation implies that a microenvironmental change of tryptophan residues takes place twice at different places of the lens proteins during normal aging. Particularly striking is that the intensity decrease of the band at 880 cm-1 proceeds in parallel with that of the Raman band at 2579 cm-1 due to a SH stretching mode for the first 4 months. Thus, the first microenvironmental change of tryptophan residues seems to be correlated with the formation of S-S bonds. In contrast to tryptophan residues, no evidence was observed of a microenvironmental change in tyrosine residues. In this respect, the structural changes of lens proteins in aging are sharply distinct from those in lens opacification, in which tyrosine as well as tryptophan residues undergo microenvironmental changes [Itoh, K., Ozaki, Y., Mizuno, A., & Iriyama, K. (1983) Biochemistry 22, 1773-1778]. The relative intensity of the band at 3390 cm-1 due to an OH stretching mode of lens water fell rapidly for the first 4 months and then decreased very gradually. The observation clearly exhibits the process of lens dehydration.(ABSTRACT TRUNCATED AT 250 WORDS)

No abstract